Literature DB >> 6499220

Polymeric complexes and fragments of albumin in normal human plasma.

B Kshirsagar, B Wilson, R C Wiggins.   

Abstract

Nitrocellulose blots of normal human plasma proteins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis were examined for polymeric complexes and fragments of albumin using an immunoperoxidase-labelled mouse monoclonal anti-human albumin antibody. Under reducing conditions, no polymeric complexes were seen. Under non-reducing conditions, polymeric complexes were detected at the following molecular weights: 210 000, 168 000, 147 000, 132 000, and 110 000. These probably represent both homo- and heteropolymers of albumin. Fresh plasma samples were also analyzed by S-200 chromatography with the same results indicating that detection of polymeric complexes was not an artifact of the sodium dodecyl sulfate-polyacrylamide gel electrophoresis technique. In quantitative terms, polymeric complexes constituted 0.3-2.8% of the total albumin present. Fragments of albumin were also seen in normal human plasma with molecular weights of 45 000, 28 000 and 19 000. These fragments probably represent breakdown products of albumin in normal blood, and they constituted less than 2% of the total albumin present.

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Year:  1984        PMID: 6499220     DOI: 10.1016/0009-8981(84)90076-7

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN: 0009-8981            Impact factor:   3.786


  5 in total

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4.  Inhibition of the metabolic degradation of filtered albumin is a major determinant of albuminuria.

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Journal:  PLoS One       Date:  2015-05-26       Impact factor: 3.240

5.  Possible Mechanisms by Which Enzymatic Degradation of Human Serum Albumin Can Lead to Bioactive Peptides and Biomarkers.

Authors:  Ulrich Kragh-Hansen
Journal:  Front Mol Biosci       Date:  2018-07-09
  5 in total

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